scholarly journals RNA determinants of translational operator recognition by the DNA polymerases of bacteriophages T4 and RB69

2002 ◽  
Vol 30 (15) ◽  
pp. 3341-3348 ◽  
Author(s):  
V. M. Petrov
Keyword(s):  
Dna Polymerases ◽  
Translational Operator

PrimPol (Primase/Polymerase), replicating enzyme – A mini review

2020 ◽  
Vol 2 (4) ◽  
pp. 89-92
Author(s):  
Muhammad Amir ◽  
Sabeera Afzal ◽  
Alia Ishaq
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Genetic Information ◽  
Nuclear Dna ◽  
De Novo ◽  
Dna Polymerases ◽  
Test Site ◽  
Mitochondrial Dna Replication ◽  
Dna Template ◽  
Preliminary Phase

Polymerases were revealed first in 1970s. Most important to the modest perception the enzyme responsible for nuclear DNA replication that was pol , for DNA repair pol and for mitochondrial DNA replication pol  DNA construction and renovation done by DNA polymerases, so directing both the constancy and discrepancy of genetic information. Replication of genome initiate with DNA template-dependent fusion of small primers of RNA. This preliminary phase in replication of DNA demarcated as de novo primer synthesis which is catalyzed by specified polymerases known as primases. Sixteen diverse DNA-synthesizing enzymes about human perspective are devoted to replication, reparation, mutilation lenience, and inconsistency of nuclear DNA. But in dissimilarity, merely one DNA polymerase has been called in mitochondria. It has been suggest that PrimPol is extremely acting the roles by re-priming DNA replication in mitochondria to permit an effective and appropriate way replication to be accomplished. Investigations from a numeral of test site have significantly amplified our appreciative of the role, recruitment and regulation of the enzyme during DNA replication. Though, we are simply just start to increase in value the versatile roles that play PrimPol in eukaryote.

DNA Polymerases and Oxidative Damage: Friends or Foes?

2008 ◽  
Vol 1 (2) ◽  
pp. 162-170 ◽  
Author(s):  
A. Amoroso ◽  
E. Crespan ◽  
U. Wimmer ◽  
U. Hubscher ◽  
G. Maga
Keyword(s):  
Oxidative Damage ◽  
Dna Polymerases

New nucleoside triphosphates modified at 5'-position, synthesis and substrate properties towards DNA polymerases

1993 ◽  
Vol 58 (s1) ◽  
pp. 120-121
Author(s):  
E. Shirokova ◽  
A. Shipitsin ◽  
E. Kusnetsova ◽  
L. Victorova ◽  
A. Krayevsky
Keyword(s):  
Dna Polymerases ◽  
Nucleoside Triphosphates ◽  
Substrate Properties ◽  
Position Synthesis

DNA-Polymerases α, δ and ε from T-Cell Spontaneous Lymphoblastic Leukemia of Sprague-Dawley Inbred Rat: Isolation and Characterization

1995 ◽  
Vol 60 (9) ◽  
pp. 1555-1572 ◽  
Author(s):  
Pavel Kramata ◽  
Jaroslav Černý ◽  
Gabriel Birkuš ◽  
Ivan Votruba ◽  
Berta Otová ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Lymphoblastic Leukemia ◽  
Dna Polymerases ◽  
Sedimentation Coefficient ◽  
Nuclear Antigen ◽  
Exonuclease Activity ◽  
Sprague Dawley ◽  
Dna Primase ◽  
Isolation And Characterization ◽  
Inbred Rat

Using a single isolation procedure and selective assays for the determination of enzyme activity, highly purified DNA-polymerases α, δ and ε were isolated from the lymphoma of Sprague-Dawley inbred rats. For pol α the subunit composition was 170, 70, 57 and 53 kDa with sedimentation coefficient 8.7 S for the native molecule; pol delta consists of two polypeptides (133 and 46 kDa; sedimentation coefficient 8.2 S), while pol ε is a single polypeptide (140 kDa) and its sedimentation coefficient is 7.0 S. Comparison of the interaction of individual enzymes with known inhibitors and proliferating cell nuclear antigen (PCNA) using the template-primer poly dA-oligo dT12-18, gave the following data: (i) pol α is selectively inhibited by N2-(p-butylphenyl)-2'-deoxyguanosine 5'-triphosphate (BuPdGTP) and stimulated by dimethyl sulfoxide; (ii) all the enzymes are inhibited by N-ethylmaleimide and aphidicolin; (iii) PCNA stimulates pol δ approximately 50 times while pol ε is moderately inhibited; (iv) pol α exhibits considerably higher DNA-primase activity with poly dC as template than with poly dT, and negligible 3'-5'-exonuclease activity whereas pol δ and pol ε, which do not exert any DNA-primase activity have approximately the same 3'-5'-exonuclease activity. The ability of individual polymerases to utilize poly dT-oligo dA12-18 as a template-primer at different pH values, ionic strengths and Mg2+-concentrations was also investigated. In comparison to poly dA-oligo dT12-18 template-primer, pol α has 140% of enzyme activity on poly dT-oligo dA12-18 under optimal conditions, whereas the activity of pol ε and pol δ is 4 times and 10 times lower, respectively.

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